Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Lea Talmann"'
Autor:
Tim Lüddecke, Anne Paas, Richard J. Harris, Lea Talmann, Kim N. Kirchhoff, André Billion, Kornelia Hardes, Antje Steinbrink, Doreen Gerlach, Bryan G. Fry, Andreas Vilcinskas
Publikováno v:
Frontiers in Bioengineering and Biotechnology, Vol 11 (2023)
Venoms are complex chemical arsenals that have evolved independently many times in the animal kingdom. Venoms have attracted the interest of researchers because they are an important innovation that has contributed greatly to the evolutionary success
Externí odkaz:
https://doaj.org/article/1790aa7987f54374b0b881d0d3578729
Autor:
Tim Lüddecke, Anne Paas, Lea Talmann, Kim N. Kirchhoff, Björn M. von Reumont, André Billion, Thomas Timm, Günter Lochnit, Andreas Vilcinskas
Publikováno v:
Toxins, Vol 13, Iss 8, p 575 (2021)
Arthropod venoms offer a promising resource for the discovery of novel bioactive peptides and proteins, but the limited size of most species translates into minuscule venom yields. Bioactivity studies based on traditional fractionation are therefore
Externí odkaz:
https://doaj.org/article/3ce23103af274c3c953882f423d9be97
Autor:
Günter Lochnit, Kim N Kirchhoff, Björn M. von Reumont, André Billion, Andreas Vilcinskas, Anne Paas, Tim Lüddecke, Thomas Timm, Lea Talmann
Publikováno v:
Toxins
Toxins, Vol 13, Iss 575, p 575 (2021)
Volume 13
Issue 8
Toxins, Vol 13, Iss 575, p 575 (2021)
Volume 13
Issue 8
Arthropod venoms offer a promising resource for the discovery of novel bioactive peptides and proteins, but the limited size of most species translates into minuscule venom yields. Bioactivity studies based on traditional fractionation are therefore
Publikováno v:
Zeitschrift für Naturforschung C. 72:405-415
Cytochrome P450 monooxygenases (P450s) are ubiquitous enzymes with a broad substrate spectrum. Insect P450s are known to catalyze reactions such as the detoxification of insecticides and the synthesis of hydrocarbons, which makes them useful for many
Autor:
Mark L. Thompson, Kristian Geitner, Marlen Schmidt, Uwe T. Bornscheuer, Lea Talmann, Maria Kadow, Stefan Saß, Dominique Böttcher
Publikováno v:
Tetrahedron. 68:7575-7580
An assay for the spectrophotometric determination of Baeyer–Villiger monooxygenase (BVMO) activity is described. Baeyer–Villiger oxidation of p-nitroacetophenone generates the corresponding acetate and subsequent hydrolysis of this ester by an es